Evidence map›Paper›PMID 26398495›Full record

ArticleKidney international2016

Renal peroxiredoxin 6 interacts with anion exchanger 1 and plays a novel role in pH homeostasis.

Sara L Sorrell, Zoe J Golder, Duncan B Johnstone, Fiona E Karet Frankl

Open access · bronzeAbstract read
In one paragraph

Article in Kidney international, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. eLife · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Knockout Mouse Models for Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2020
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Sara L Sorrell *Department of Medical Genetics, University of Cambridge, Cambridge, United Kingdom.
Zoe J Golder *Department of Medical Genetics, University of Cambridge, Cambridge, United Kingdom.
Duncan B JohnstoneSection of Nephrology, Hypertension and Kidney Transplantation, School of Medicine, Temple University, Philadelphia, PA, USA.
Fiona E Karet FranklDepartment of Medical Genetics, University of Cambridge, Cambridge, United Kingdom.
University of Cambridge · GBTemple University · US

Funding

Wellcome Trust 066438Wellcome Trust 079895Wellcome Trust 088489Wellcome Trust 088489/Z/09/ZWellcome Trust 100140Wellcome Trust 100140/Z/12/Z
6 · The paper itself

Abstract

Peroxiredoxin 6 (PRDX6) is one of the six members of the PRDX family, which have peroxidase and antioxidant activity. PRDX6 is unique, containing only one conserved cysteine residue (C47) rather than the two found in other PRDXs. A yeast two-hybrid screen found PRDX6 to be a potential binding partner of the C-terminal tail of anion exchanger 1 (AE1), a Cl(-)/HCO(3)(-) exchanger basolaterally expressed in renal α-intercalated cells. PRDX6 immunostaining in human kidney was both cytoplasmic and peripheral and colocalized with AE1. Analysis of native protein showed that it was largely monomeric, whereas expressed tagged protein was more dimeric. Two methionine oxidation sites were identified. In vitro and ex vivo pull-downs and immunoprecipitation assays confirmed interaction with AE1, but mutation of the conserved cysteine resulted in loss of interaction. Prdx6 knockout mice had a baseline acidosis with a major respiratory component and greater AE1 expression than wild-type animals. After an oral acid challenge, PRDX6 expression increased in wild-type mice, with preservation of AE1. However, AE1 expression was significantly decreased in knockout animals. Kidneys from acidified mice showed widespread proximal tubular vacuolation in wild-type but not knockout animals. Knockdown of PRDX6 by siRNA in mammalian cells reduced both total and cell membrane AE1 levels. Thus, PRDX6-AE1 interaction contributes to the maintenance of AE1 during cellular stress such as during metabolic acidosis.

Indexed as

AcidosisAnimalsAnion Exchange Protein 1, ErythrocyteHomeostasisHumansHydrogen-Ion ConcentrationImmunohistochemistryImmunoprecipitationKidneyMiceMice, KnockoutPeroxiredoxin VIAnion Exchange Protein 1, ErythrocytePeroxiredoxin VIacidosisAE1cellular stressdistal tubulePRDX6renal pathology

Identifiers

PMID26398495
PMCPMC4705439
OpenAlexW2193475846

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.